B2JVU2 · FTSH_PARP8

Function

function

Acts as a processive, ATP-dependent zinc metallopeptidase for both cytoplasmic and membrane proteins. Plays a role in the quality control of integral membrane proteins.

Cofactor

Zn2+ (UniProtKB | Rhea| CHEBI:29105 )

Note: Binds 1 zinc ion per subunit.

Features

Showing features for binding site, active site.

164550100150200250300350400450500550600
TypeIDPosition(s)Description
Binding site199-206ATP (UniProtKB | ChEBI)
Binding site423Zn2+ (UniProtKB | ChEBI); catalytic
Active site424
Binding site427Zn2+ (UniProtKB | ChEBI); catalytic
Binding site500Zn2+ (UniProtKB | ChEBI); catalytic

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentplasma membrane
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionATP-dependent peptidase activity
Molecular Functionmetalloendopeptidase activity
Molecular Functionzinc ion binding
Biological Processprotein catabolic process
Biological Processproteolysis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    ATP-dependent zinc metalloprotease FtsH
  • EC number

Gene names

    • Name
      ftsH
    • Ordered locus names
      Bphy_6007

Encoded on

  • Plasmid pBPHY01

Organism names

Accessions

  • Primary accession
    B2JVU2

Proteomes

Subcellular Location

Cell inner membrane
; Multi-pass membrane protein

Features

Showing features for topological domain, transmembrane.

TypeIDPosition(s)Description
Topological domain1-8Cytoplasmic
Transmembrane9-29Helical
Topological domain30-105Periplasmic
Transmembrane106-126Helical
Topological domain127-645Cytoplasmic

Keywords

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00004003331-645ATP-dependent zinc metalloprotease FtsH

Interaction

Subunit

Homohexamer.

Structure

Family & Domains

Features

Showing features for region, compositional bias.

TypeIDPosition(s)Description
Region612-645Disordered
Compositional bias623-637Basic and acidic residues

Sequence similarities

In the central section; belongs to the AAA ATPase family.
In the C-terminal section; belongs to the peptidase M41 family.

Keywords

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    645
  • Mass (Da)
    69,090
  • Last updated
    2008-06-10 v1
  • Checksum
    10C0CACB4F0F3B46
MDFNREHKINFLYVLAAMVGVLLIQSLVSQPDHIRTIPYSEFQQLASQGKVTDLVVGPTRITGTLKDAPKDSPRHFSTLRVDQALAQSLTNENVTFSGEPEPGPWPTILGWLMPIVGFALVWMFLIRPMSMGPGMDGMMSIGKSKARVYVEKDIKVTFADVAGVDEAKDELKEVVSFLRDPRSYGRLGARVPKGVLLVGPPGTGKTLLARAVAGEAGVAFFSISGSEFVEMFVGVGAARVRDLFEQARKHAPAIVFIDELDSLGRARGSAFPGGGGHDEKEQTLNQLLAELDGFDTSIGVVLLAATNRPEILDPALLRAGRFDRQVLVDRPDKKGRAQILEVHLKKIALAPGVPVDDIAALTPGFSGADLANLVNEAAILATRRHAENVSLDDFTQAIERIVAGLEKRNRLLNAHEREVVAHHEMGHALVAMTLPGVDMVQKISIIPHGIAALGYTIQRPTEERFLMDRAELMNRMAVLLGGRAAERLIFADVSTGAADDLAKASAIARSMVVRFGMDPTLGQVAYEPETTSALGLPNGSEWRPRQYGEQTAAAIDAAVRELIETASACAFSILQANRGLLESAARDLLAKETMSGEELQALLSQLGGGAASASVLRDGGDGAADAGQDRSGEHRALTVEGGEAQ

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias623-637Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
CP001045
EMBL· GenBank· DDBJ
ACC75069.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp